The evolution of peroxisomal and mitochondrial alanine: Glyoxylate aminotransferase 1 in mammalian liver

Yoshikazu Takada; Tomoo Noguchi

doi:10.1016/0006-291X(82)91844-7

The evolution of peroxisomal and mitochondrial alanine: Glyoxylate aminotransferase 1 in mammalian liver

Yoshikazu Takada, Tomoo Noguchi

Research output: Contribution to journal › Article › peer-review

12 Citations (Scopus)

Abstract

Immunological distances of alanine: glyoxylate aminotransferase 1 (serine:pyruvate aminotransferase) in mitochondria or peroxisomes from eight different mammalian liver were determined with rabbit anti-serum against the mitochondrial enzyme of rat liver by microcomplement fixation. Results suggest that heterotopic alanine:glyoxylate aminotransferase 1 are orthologous proteins and their subcellular localization and substrate specificity changed during rapid molecular evolution.

Original language	English
Pages (from-to)	153-157
Number of pages	5
Journal	Biochemical and Biophysical Research Communications
Volume	108
Issue number	1
DOIs	https://doi.org/10.1016/0006-291X(82)91844-7
Publication status	Published - Sept 16 1982
Externally published	Yes

ASJC Scopus subject areas

Molecular Biology
Biophysics
Biochemistry
Cell Biology

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10.1016/0006-291X(82)91844-7

Cite this

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title = "The evolution of peroxisomal and mitochondrial alanine: Glyoxylate aminotransferase 1 in mammalian liver",

abstract = "Immunological distances of alanine: glyoxylate aminotransferase 1 (serine:pyruvate aminotransferase) in mitochondria or peroxisomes from eight different mammalian liver were determined with rabbit anti-serum against the mitochondrial enzyme of rat liver by microcomplement fixation. Results suggest that heterotopic alanine:glyoxylate aminotransferase 1 are orthologous proteins and their subcellular localization and substrate specificity changed during rapid molecular evolution.",

author = "Yoshikazu Takada and Tomoo Noguchi",

year = "1982",

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doi = "10.1016/0006-291X(82)91844-7",

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T1 - The evolution of peroxisomal and mitochondrial alanine

T2 - Glyoxylate aminotransferase 1 in mammalian liver

AU - Takada, Yoshikazu

AU - Noguchi, Tomoo

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Y1 - 1982/9/16

N2 - Immunological distances of alanine: glyoxylate aminotransferase 1 (serine:pyruvate aminotransferase) in mitochondria or peroxisomes from eight different mammalian liver were determined with rabbit anti-serum against the mitochondrial enzyme of rat liver by microcomplement fixation. Results suggest that heterotopic alanine:glyoxylate aminotransferase 1 are orthologous proteins and their subcellular localization and substrate specificity changed during rapid molecular evolution.

AB - Immunological distances of alanine: glyoxylate aminotransferase 1 (serine:pyruvate aminotransferase) in mitochondria or peroxisomes from eight different mammalian liver were determined with rabbit anti-serum against the mitochondrial enzyme of rat liver by microcomplement fixation. Results suggest that heterotopic alanine:glyoxylate aminotransferase 1 are orthologous proteins and their subcellular localization and substrate specificity changed during rapid molecular evolution.

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AN - SCOPUS:0020485238

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ER -

The evolution of peroxisomal and mitochondrial alanine: Glyoxylate aminotransferase 1 in mammalian liver

Abstract

ASJC Scopus subject areas

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